5KOR: Arabidopsis Thaliana Fucosyltransferase 1 (fut1) In Complex With Gdp And A Xylo-oligossacharide

Citation:
Abstract
The plant cell wall is a complex and dynamic network made mostly of cellulose, hemicelluloses, and pectins. Xyloglucan, the major hemicellulosic component in Arabidopsis thaliana, is biosynthesized in the Golgi apparatus by a series of glycan synthases and glycosyltransferases before export to the wall. A better understanding of the xyloglucan biosynthetic machinery will give clues toward engineering plants with improved wall properties or designing novel xyloglucan-based biomaterials. The xyloglucan-specific alpha2-fucosyltransferase FUT1 catalyzes the transfer of fucose from GDP-fucose to terminal galactosyl residues on xyloglucan side chains. Here, we present crystal structures of Arabidopsis FUT1 in its apoform and in a ternary complex with GDP and a xylo-oligosaccharide acceptor (named XLLG). Although FUT1 is clearly a member of the large GT-B fold family, like other fucosyltransferases of known structures, it contains a variant of the GT-B fold. In particular, it includes an extra C-terminal region that is part of the acceptor binding site. Our crystal structures support previous findings that FUT1 behaves as a functional dimer. Mutational studies and structure comparison with other fucosyltransferases suggest that FUT1 uses a SN2-like reaction mechanism similar to that of protein-O-fucosyltransferase 2. Thus, our results provide new insights into the mechanism of xyloglucan fucosylation in the Golgi.
PDB ID: 5KORDownload
MMDB ID: 144009
PDB Deposition Date: 2016/7/1
Updated in MMDB: 2016/11
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 5KOR: dimeric; determined by author
Molecular Components in 5KOR
Label Count Molecule
Proteins (2 molecules)
2
Galactoside 2-alpha-l-fucosyltransferase(Gene symbol: FT1)
Molecule annotation
Chemicals (15 molecules)
1
2
2
4
3
3
4
4
5
1
6
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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